da Silva, Luis Pinto; Vieira, Joao; Esteves da Silva, Joaquim C. G.
Comparative theoretical study of the binding of luciferyl-adenylate and dehydroluciferyl-adenylate to firefly luciferase
CHEMICAL PHYSICS LETTERS, 543:137-141, AUG 10 2012

This is the first report of a study employing a computational approach to study the binding of (D/L)-luciferyl-adenlyates and dehydroluciferyl-adenylate to firefly luciferase. A semi-empirical/molecular mechanics methodology was used to study the interaction between these ligands and active site molecules. All adenylates are complexed with the enzyme, mostly due to electrostatic interactions with cationic residues. Dehydroluciferyl-adenylate is expected to be a competitive inhibitor of luciferyl-adenylate, as their binding mechanism and affinity to luciferase are very similar. Both luciferyl-adenylates adopt the L-orientation in the active site of luciferase. (C) 2012 Elsevier B.V. All rights reserved.

DOI:10.1016/j.cplett.2012.06.038

Find full text with Google Scholar.